[en] It is shown that a small subset of modes which are likely to be involved in protein functional motions of
large amplitude can be determined by retaining the most robust normal modes obtained using different
protein models. This result should prove helpful in the context of several applications proposed recently,
like for solving difficult molecular replacement problems or for fitting atomic structures into low-
resolution electron density maps. It may also pave the way for the development of methods allowing
us to predict such motions accurately.
Disciplines :
Mathematics
Author, co-author :
Nicolay, Samuel ; Université de Liège - ULiège > Département de mathématique > Analyse - Analyse fonctionnelle - Ondelettes
Sanejouand, Y. H.
Language :
English
Title :
Functional modes of proteins are among the most robust
Publication date :
2004
Journal title :
Physical Review Letters
ISSN :
0031-9007
eISSN :
1079-7114
Publisher :
American Physical Society, Ridge, United States - New York
scite shows how a scientific paper has been cited by providing the context of the citation, a classification describing whether it supports, mentions, or contrasts the cited claim, and a label indicating in which section the citation was made.
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